28118-35-6Relevant academic research and scientific papers
Oxidation of putrescine and cadaverine derivatives by diamine oxidases
Equi, Angela M.,Brown, Alison M.,Cooper, Alan,Her, Surjit K.,Watson, Allan B.,Robins, David J.
, p. 507 - 518 (2007/10/02)
A range of putrescine and cadaverine derivatives has been synthesized and assayed as substrates for the diamine oxidases from pea seedlings and pig kidney. KM and Vmax data are reported, mainly for the pea enzyme. N-Alkylputrescines and C-alkylcadaverines are generally poorer substrates than the parent compounds with up to 4500-fold reduction in Vmax. There is significantly less variation in KM values, indicating that the binding site of the pea enzyme is relatively non-specific and that enzymic specificity lies at the catalytic stage. This suggests that poor substrates might act as convenient, short-lived inhibitors of diamine oxidases.
SYNTHESIS AND 13C-NMR CHARACTERISATION OF NEW C-SUBSTITUTED 1,3-DICYANOPROPANES
Brunelli, Maurizio,Prevedello, Aldo
, p. 247 - 252 (2007/10/02)
New dinitriles of the general formula NC-CR1R2-CR3R4-CH2-CN have been prepared by reaction of aliphatic nitriles with unsaturated nitriles. 13C-NMR spectra of the compounds with one chiral centre show split resonance lines for the α equivalent methyls.The compounds with two chiral centres show separate sets of signals for the racemic erythro and threo forms.
